2VUS

Crystal structure of unliganded NmrA-AreA zinc finger complex

Summary for 2VUS

• Entry DOI: 10.2210/pdb2vus/pdb
• Related: 2VUT 2VUU
• Descriptor: NITROGEN METABOLITE REPRESSION REGULATOR NMRA, NITROGEN REGULATORY PROTEIN AREA, SULFATE ION, ... (6 entities in total)
• Functional Keywords: transcription regulation, protein-protein interactions, metal-binding, nitrate assimilation, zinc-finger, dna-binding, zinc fingers, transcription, zinc, area, nmra, nucleus, activator, gata-type
• Biological source: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans); More
• Cellular location: Nucleus: P17429
• Total number of polymer chains: 16
• Total formula weight: 350538.68

Authors

Kotaka, M.,Johnson, C.,Lamb, H.K.,Hawkins, A.R.,Ren, J.,Stammers, D.K. (deposition date: 2008-05-30, release date: 2008-07-29, Last modification date: 2024-05-08)

Primary citation

Kotaka, M.,Johnson, C.,Lamb, H.K.,Hawkins, A.R.,Ren, J.,Stammers, D.K.
Structural Analysis of the Recognition of the Negative Regulator Nmra and DNA by the Zinc Finger from the Gata-Type Transcription Factor Area.
J.Mol.Biol., 381:373-, 2008

PubMed Abstract: Amongst the most common protein motifs in eukaryotes are zinc fingers (ZFs), which, although largely known as DNA binding modules, also can have additional important regulatory roles in forming protein:protein interactions. AreA is a transcriptional activator central to nitrogen metabolism in Aspergillus nidulans. AreA contains a GATA-type ZF that has a competing dual recognition function, binding either DNA or the negative regulator NmrA. We report the crystal structures of three AreA ZF-NmrA complexes including two with bound NAD(+) or NADP(+). The molecular recognition of AreA ZF-NmrA involves binding of the ZF to NmrA via hydrophobic and hydrogen bonding interactions through helices alpha1, alpha6 and alpha11. Comparison with an earlier NMR solution structure of AreA ZF-DNA complex by overlap of the AreA ZFs shows that parts of helices alpha6 and alpha11 of NmrA are positioned close to the GATA motif of the DNA, mimicking the major groove of DNA. The extensive overlap of DNA with NmrA explains their mutually exclusive binding to the AreA ZF. The presence of bound NAD(+)/NADP(+) in the NmrA-AreaA ZF complex, however, causes minimal structural changes. Thus, any regulatory effects on AreA function mediated by the binding of oxidised nicotinamide dinucleotides to NmrA in the NmrA-AreA ZF complex appear not to be modulated via protein conformational rearrangements.

PubMed: 18602114
DOI: 10.1016/J.JMB.2008.05.077

Experimental method

X-RAY DIFFRACTION (2.6 Å)